MolNFT v1 · #139373 · protein
Crystal structure of human deah-box RNA helicase DHX15 in complex with ADP
5XDR · Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15: “Crystal structure of human deah-box RNA helicase DHX15 in complex with ADP”. X-ray diffraction, 3 ligands (ADP, MG, SO4), 10 pockets (best druggability 0.84). MolNFT v1…
- PDB
- 5XDR
- Type
- protein
- Length
- 679 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15
- EC
- 3.6.4.13
- UniProt
- O43143
- Ligands
- ADP, MG, SO4
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 (EC 3.6.4.13) | protein | 679 | 40% helix, 19% strand | O43143 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.84 | 0.85 | 106 | empty |
| 2 | 256 | 0.69 | 0.85 | 32 | ADP, MG |
| 3 | 68 | 0.61 | 0.90 | 23 | empty |
| 4 | 89 | 0.60 | 0.88 | 19 | empty |
| 5 | 142 | 0.49 | 0.78 | 18 | empty |
Compared structures
- 5XDR · Crystal structure of human DEAH-box RNA helicase DHX15 in complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
- O43143 · AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor ATP- dependent RNA… · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O43143
- Elsewhere: RCSB PDB 5XDR · PDBe 5XDR · UniProt O43143
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